Structural and biochemical characterization of FK506 binding protein (FKBP) from plasmodium falciparum any) plasmodium vivax.

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Bibliographic Details
Main Author:	Reema Alag
Other Authors:	Yoon Ho Sup
Format:	Theses and Dissertations
Published:	2014
Subjects:	DRNTU::Science::Biological sciences::Microbiology
Online Access:	http://hdl.handle.net/10356/57415
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Institution:	Nanyang Technological University

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spelling	sg-ntu-dr.10356-574152023-02-28T18:46:48Z Structural and biochemical characterization of FK506 binding protein (FKBP) from plasmodium falciparum any) plasmodium vivax. Reema Alag Yoon Ho Sup School of Biological Sciences DRNTU::Science::Biological sciences::Microbiology 162 p. Plasmodium falciparum and Plasmodium vivax are two major malaria causing species and develop resistance to currently available antimalarial drugs. This prompts a need to identify parasitic proteins that could serve as novel targets to design antimalarial drugs. Previous studies have demonstrated that FK506 and rapamycin exhibit antimalarial effects, suggesting the presence of FK506 binding protein (FKBP) homolog in the parasite. Recently FKBP protein with molecular weight of 35 kDa has been identified in P. falciparum (P/FKBP35) and its homolog in P. vivax was also identified by our group (PvFKBP35). FK506 binding protein (FKBP) family is one of the major families of immunophilins, which binds to the immunosuppressive drug FK506. FKBPs are largely distributed in different eukaryotes and perform important physiological functions. FKBPs show peptidylprolyl cis-trans isomerase (PPIase) and chaperonic activities. FKBPs also act as co-chaperones and interact with Hsp90, suggesting the role of FKBPs in protein folding and assembly of proteins. P/FKBP35 and PvFKBP35 consist of N-terminal FK506 binding domain (FKBD) followed by tetratricopeptide repeats (TPR) domain and calmodulin binding domain (CaM). Genome analysis of P. falciparum and P. vivax revealed the presence of only one FKBP protein in the parasites. P/FKBP35 and PvFKBP35 proteins could be important for physiological functions of the parasite. Currently, the role and function of the proteins in the parasites remain to be further explored. Doctor of Philosophy (SBS) 2014-04-07T10:30:59Z 2014-04-07T10:30:59Z 2011 2011 Thesis http://hdl.handle.net/10356/57415 Nanyang Technological University application/pdf
institution	Nanyang Technological University
building	NTU Library
continent	Asia
country	Singapore Singapore
content_provider	NTU Library
collection	DR-NTU
topic	DRNTU::Science::Biological sciences::Microbiology
spellingShingle	DRNTU::Science::Biological sciences::Microbiology Reema Alag Structural and biochemical characterization of FK506 binding protein (FKBP) from plasmodium falciparum any) plasmodium vivax.
description	162 p.
author2	Yoon Ho Sup
author_facet	Yoon Ho Sup Reema Alag
format	Theses and Dissertations
author	Reema Alag
author_sort	Reema Alag
title	Structural and biochemical characterization of FK506 binding protein (FKBP) from plasmodium falciparum any) plasmodium vivax.
title_short	Structural and biochemical characterization of FK506 binding protein (FKBP) from plasmodium falciparum any) plasmodium vivax.
title_full	Structural and biochemical characterization of FK506 binding protein (FKBP) from plasmodium falciparum any) plasmodium vivax.
title_fullStr	Structural and biochemical characterization of FK506 binding protein (FKBP) from plasmodium falciparum any) plasmodium vivax.
title_full_unstemmed	Structural and biochemical characterization of FK506 binding protein (FKBP) from plasmodium falciparum any) plasmodium vivax.
title_sort	structural and biochemical characterization of fk506 binding protein (fkbp) from plasmodium falciparum any) plasmodium vivax.
publishDate	2014
url	http://hdl.handle.net/10356/57415
_version_	1759857204428537856

Structural and biochemical characterization of FK506 binding protein (FKBP) from plasmodium falciparum any) plasmodium vivax.

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